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mDia induces circumferential actin filaments around the edge of the synaptic cleft, which contract the presynaptic terminals in a ROCK-dependent manner.
these results uncover a novel role for mDia1 in Abeta-mediated synaptotoxicity and demonstrate that inhibition of MT dynamics and accumulation of PTMs are driving factors for the induction of tau-mediated neuronal damage.
Small Molecule Inhibition of Ligand-Stimulated RAGE (show AGER Proteins)-DIAPH1 Signal Transduction.
Diaphanous-related formin (show DIAPH3 Proteins) signaling plays a role in heart and vascular development and the maintenance of SMC (show DYM Proteins) phenotype.
Liprin-alpha3 (show PPFIA3 Proteins) uses an alpha-helical region to bind to mDia1, counteracting mouse Dia1 (show CYB5R3 Proteins) activation by RhoA (show RHOA Proteins).
Depleting FMNL1 (show FMNL1 Proteins), another Formin (show FMN1 Proteins) family member, resulted in reduced mDia1 expression, while RhoA (show RHOA Proteins) inhibition did not alter mDia1 expression, which indicated that there was a FMNL1 (show FMNL1 Proteins)-mDia1-Profilin1 (show PFN1 Proteins) signaling pathway in mouse oocytes.
Mechanistically, mDia1 deficiency led to a downregulation of membrane-associated genes and a specific upregulation of CD14 (show CD14 Proteins) messenger RNA in granulocytes, but not in other lineages.
Mammalian diaphanous-related formin 1 regulates GSK3beta-dependent microtubule dynamics required for T cell migratory polarization.
mDia1 can efficiently put actin filaments under mechanical tension.
The active form of mDia1 localized to the apical membrane in exocrine pancreas cells; introduction of an active form of mDia1 leads to a marked increase in actin bundle density along the secretory vesicle lumen perimeter.
mDia1 was recruited to the zonula adherens (ZA) of established Caco-2 monolayers in response to E-cadherin (show CDH1 Proteins) and RhoA (show RHOA Proteins).
Actin dynamics and formins control DNA replication by multiple direct and indirect mechanisms.
DIAPH1 interaction with the RAGE (show AGER Proteins) cytoplasmic domain. [review]
Ligand-induced association of RAGE (show AGER Proteins) homodimers on the cell surface increases the molecular dimension of the receptor, recruiting DIAPH1 and activating signaling pathways.
The authors describe a novel patient-derived DIAPH1 mutation (c.3610C>T) in two unrelated families, which results in early termination prior to a basic amino acid motif (RRKR(1204-1207)) at the DAD C-terminus. The mutant DIA1 (show CYB5R3 Proteins)(R1204X) disrupted the autoinhibitory DID-DAD interaction and was constitutively active.
The description of a novel disorder of platelet formation and hearing loss extends the repertoire of DIAPH1-related disease, and provides new insight into the autoregulation of DIAPH1 activity.
Studies indicate that diaphanous related formin 1 (DIAPH1) is essentially involved in microtubules (MTs (show TIMM8A Proteins))-dependent early adhesion of colon cancer cells.
A 51-year-old patient in a Korean family with ADNSHL was examined by pure-tone audiometry, and genetic analysis of DIAPH1 was performed. A novel variant, p.I530S (c.1589T > G), was identified in the DIAPH1 gene, and the mutation was located in the highly conserved coiled-coil domain of the DIA1 (show CYB5R3 Proteins) protein.
mDia1 is an important regulator of breast cancer cell invasion and that its effects may be mediated by MMP-2 (show MMP2 Proteins) activity.
Findings suggest that regulation of cellular trafficking and microtubule-mediated localization of MT1-MMP (show MMP14 Proteins) by mDia1 is likely important in breast cancer invasion through the expression of cancer stem cell genes.
This gene is a homolog of the Drosophila diaphanous gene, and has been linked to autosomal dominant, fully penetrant, nonsyndromic sensorineural progressive low-frequency hearing loss. Actin polymerization involves proteins known to interact with diaphanous protein in Drosophila and mouse. It has therefore been speculated that this gene may have a role in the regulation of actin polymerization in hair cells of the inner ear. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
diaphanous homolog 1 (Drosophila)
, diaphanous homolog 1
, diaphanous homolog 2
, protein diaphanous homolog 1
, protein diaphanous homolog 1-like
, diaphanous-related formin-1